| UniProt ID | A1BG_HUMAN | |
|---|---|---|
| UniProt AC | P04217 | |
| Protein Name | Alpha-1B-glycoprotein | |
| Gene Name | A1BG | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 495 | |
| Subcellular Localization | Secreted. | |
| Protein Description | ||
| Protein Sequence | MSMLVVFLLLWGVTWGPVTEAAIFYETQPSLWAESESLLKPLANVTLTCQAHLETPDFQLFKNGVAQEPVHLDSPAIKHQFLLTGDTQGRYRCRSGLSTGWTQLSKLLELTGPKSLPAPWLSMAPVSWITPGLKTTAVCRGVLRGVTFLLRREGDHEFLEVPEAQEDVEATFPVHQPGNYSCSYRTDGEGALSEPSATVTIEELAAPPPPVLMHHGESSQVLHPGNKVTLTCVAPLSGVDFQLRRGEKELLVPRSSTSPDRIFFHLNAVALGDGGHYTCRYRLHDNQNGWSGDSAPVELILSDETLPAPEFSPEPESGRALRLRCLAPLEGARFALVREDRGGRRVHRFQSPAGTEALFELHNISVADSANYSCVYVDLKPPFGGSAPSERLELHVDGPPPRPQLRATWSGAVLAGRDAVLRCEGPIPDVTFELLREGETKAVKTVRTPGAAANLELIFVGPQHAGNYRCRYRSWVPHTFESELSDPVELLVAES | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 37 | Phosphorylation | SLWAESESLLKPLAN CHHCCCHHHHHHHCC | 48.56 | 24719451 | |
| 44 | N-linked_Glycosylation | SLLKPLANVTLTCQA HHHHHHCCCEEEEEE | 34.68 | 19838169 | |
| 44 | N-linked_Glycosylation | SLLKPLANVTLTCQA HHHHHHCCCEEEEEE | 34.68 | 14760718 | |
| 179 | N-linked_Glycosylation | FPVHQPGNYSCSYRT CCCCCCCCCEEEEEC | 32.03 | 18638581 | |
| 179 | N-linked_Glycosylation | FPVHQPGNYSCSYRT CCCCCCCCCEEEEEC | 32.03 | 14760718 | |
| 198 | O-linked_Glycosylation | ALSEPSATVTIEELA CCCCCCEEEEHHHHC | 23.63 | OGP | |
| 363 | N-linked_Glycosylation | EALFELHNISVADSA HHHHHEECCCHHHCC | 40.63 | 16335952 | |
| 363 | N-linked_Glycosylation | EALFELHNISVADSA HHHHHEECCCHHHCC | 40.63 | 16335952 | |
| 371 | N-linked_Glycosylation | ISVADSANYSCVYVD CCHHHCCCCEEEEEE | 32.95 | 16335952 | |
| 371 | N-linked_Glycosylation | ISVADSANYSCVYVD CCHHHCCCCEEEEEE | 32.95 | 16335952 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of A1BG_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of A1BG_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of A1BG_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MRP6_HUMAN | ABCC6 | physical | 21988832 | |
| PRDX4_HUMAN | PRDX4 | physical | 21988832 | |
| SETD7_HUMAN | SETD7 | physical | 21988832 | |
| ZBT40_HUMAN | ZBTB40 | physical | 28514442 | |
| PSME4_HUMAN | PSME4 | physical | 28514442 | |
| UBAC1_HUMAN | UBAC1 | physical | 28514442 | |
| WDR62_HUMAN | WDR62 | physical | 28514442 | |
| KCMF1_HUMAN | KCMF1 | physical | 28514442 | |
| RN123_HUMAN | RNF123 | physical | 28514442 | |
| UBR4_HUMAN | UBR4 | physical | 28514442 | |
| UBXN1_HUMAN | UBXN1 | physical | 28514442 | |
| ADRO_HUMAN | FDXR | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Enrichment of glycopeptides for glycan structure and attachment siteidentification."; Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.; Nat. Methods 6:809-811(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY. | |
| "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44; ASN-179; ASN-363 ANDASN-371, AND MASS SPECTROMETRY. | |
| "Screening for N-glycosylated proteins by liquid chromatography massspectrometry."; Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; Proteomics 4:454-465(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-44 AND ASN-179, AND MASSSPECTROMETRY. | |
| "Amino acid sequence of human plasma alpha 1B-glycoprotein: homologyto the immunoglobulin supergene family."; Ishioka N., Takahashi N., Putnam F.W.; Proc. Natl. Acad. Sci. U.S.A. 83:2363-2367(1986). Cited for: PROTEIN SEQUENCE OF 22-495, DISULFIDE BONDS, GLYCOSYLATION AT ASN-44;ASN-179; ASN-363 AND ASN-371, AND VARIANT ARG-52. | |